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. 2018 Jan 31;8:1960. doi: 10.1038/s41598-018-20290-8

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Binding of Tarp to actin. Left: The chemical shift perturbations (∆δ) (top) and relative peak intensity changes (bottom) observed between [¹H-¹⁵N]-HSQC spectra of free Tarp_726–825 and those containing 0.8:1 (black) and 2:1 (red) approximate molar ratios of G-actin. The residues highlighted within the green strip indicate the WH2-homologous Tarp region (residues 746–767) used for the Rosetta based FlexPepDock modeling^26,27. Top right: The 10 lowest energy complex models of the docked Tarp WH2 region (green) with actin using the FlexPepDock webserver. The actin surface was coloured by electrostatic charge (−3 (red) to +3 kT.e⁻¹ (blue)) using the APBS plugin⁵⁶ for PyMOL (The PyMOL Molecular Graphics System, Version 1.8.2 Schrödinger, LLC). Bottom right: The lowest energy docked Tarp:actin complex, with labeled residues, compared to the WAVE2 (pdb code: 2A40) structure (cyan) with a red transparent actin surface.